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'''Unreleased structure'''
==Crystal structure of Octaprenyl Pyrophosphate synthase from Escherichia coli with farnesyl S-thiol-pyrophosphate (FSPP)==
<StructureSection load='3wjn' size='340' side='right' caption='[[3wjn]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wjn]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WJN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WJN FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FPS:S-[(2E,6E)-3,7,11-TRIMETHYLDODECA-2,6,10-TRIENYL]+TRIHYDROGEN+THIODIPHOSPHATE'>FPS</scene><br>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wjk|3wjk]], [[3wjo|3wjo]]</td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wjn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wjn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wjn RCSB], [http://www.ebi.ac.uk/pdbsum/3wjn PDBsum]</span></td></tr>
<table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Octaprenyl pyrophosphate synthase (OPPs) catalyzes consecutive condensation reactions of one allylic substrate farnesyl pyrophosphate (FPP) and five homoallylic substrate isopentenyl pyrophosphate (IPP) molecules to form a C40 long-chain product OPP, which serves as a side chain of ubiquinone and menaquinone. OPPs belongs to the trans-prenyltransferase class of proteins. The structures of OPPs from Escherichia coli were solved in the apo-form as well as in complexes with IPP and a FPP thio-analog, FsPP, at resolutions of 2.2 to 2.6 A, and revealed the detailed interactions between the ligands and enzyme. At the bottom of the active-site tunnel, M123 and M135 act in concert to form a wall which determines the final chain length. These results represent the first ligand-bound crystal structures of a long-chain trans-prenyltransferase and provide new information on the mechanisms of catalysis and product chain elongation. (c) Proteins 2014;. (c) 2014 Wiley Periodicals, Inc.


The entry 3wjn is ON HOLD  until Paper Publication
Crystal structures of ligand-bound octaprenyl pyrophosphate synthase from escherichia coli reveal the catalytic and chain-length determining mechanisms.,Han X, Chen CC, Kuo CJ, Huang CH, Zheng Y, Ko TP, Zhu Z, Feng X, Wang K, Oldfield E, Wang AH, Liang PH, Guo RT, Ma Y Proteins. 2014 Jun 4. doi: 10.1002/prot.24618. PMID:24895191<ref>PMID:24895191</ref>


Authors: Han, X., Chen, C.C., Kuo, C.J., Huang, C.H., Zheng, Y., Ko, T.P., Zhu, Z., Feng, X., Oldfield, E., Liang, P.H., Guo, R.T., Ma, Y.H.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: Crystal structure of Octaprenyl Pyrophosphate synthase from Escherichia coli with farnesyl S-thiol-pyrophosphate (FSPP)
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chen, C C.]]
[[Category: Feng, X.]]
[[Category: Guo, R T.]]
[[Category: Han, X.]]
[[Category: Huang, C H.]]
[[Category: Ko, T P.]]
[[Category: Kuo, C J.]]
[[Category: Liang, P H.]]
[[Category: Ma, Y H.]]
[[Category: Oldfield, E.]]
[[Category: Zheng, Y.]]
[[Category: Zhu, Z.]]
[[Category: Prenyltransferase]]
[[Category: Product chain length]]
[[Category: Site-directed mutagenesis]]
[[Category: Transferase]]
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